PEDS Advance Access published online on March 24, 2006
Protein Engineering Design and Selection, doi:10.1093/protein/gzl009
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1 Bioinformatics Program, University of the Sciences in Philadelphia, Philadelphia, PA 19104, USA
* To whom correspondence should be addressed. Evolutionarily conserved hydrophobic residues at the core of protein structures are generally assumed to play a structural role in protein folding and stability. Recent studies have implicated that their importance to protein structures is uneven, with a few of them being crucial and the rest of them being secondary. In this work, we explored the possibility of employing this feature of native structures for discriminating non-native structures from native ones. First, we developed a network tool to quantitatively measure the structural contributions of individual amino acid residues. We systematically applied this method to diverse fold-type sets of native proteins. It was confirmed that this method could grasp the essential structural features of native proteins. Next, we applied it to a number of decoy sets of proteins. The results indicate that such an approach indeed identified non-native structures in most test cases. This finding should be of help for the investigation of the fundamental problem of protein structure prediction.
Received October 18, 2005
Revised February 1, 2006
Accepted February 21, 2006
Article
A simple approach for protein structure discrimination based on the network pattern of conserved hydrophobic residues
Usha K. Muppirala 1
and
Zhijun Li 2 *
2 Bioinformatics Program, University of the Sciences in Philadelphia, Philadelphia, PA 19104, USA; Department of Chemistry & Biochemistry, University of the Sciences in Philadelphia, Philadelphia, PA 19104, USA
Zhijun Li, E-mail: z.li{at}usip.edu
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